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A new method to visualize the helicobacter pylori-associated lewisb-binding adhesin utilizing SDS-digested freeze-fracture replica labeling
Linköping University, Department of Molecular and Clinical Medicine, Medical Microbiology. Linköping University, Faculty of Health Sciences.
Linköping University, Department of Molecular and Clinical Medicine, Medical Microbiology. Linköping University, Faculty of Health Sciences.
Department of Odontology, Umeå University, Umeå, Sweden .
Department of Odontology, Umeå University, Umeå, Sweden .
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2000 (English)In: Journal of Histochemistry and Cytochemistry, ISSN 0022-1554, E-ISSN 1551-5044, Vol. 48, no 6, 877-883 p.Article in journal (Refereed) Published
Abstract [en]

Freeze-fracture replica labeling has become a versatile tool to visualize both membrane components and other cell structures using SDS-replica cleaning before specific immunogold labeling of proteins or lipids. We report here for the first time the adoption and optimization of the method to studies of bacterial envelopes, as applied to structural analysis of the distribution of the unique BabA-adhesin of the gastric pathogen Helicobacter pylori. BabA is important for bacterial adherence to the human epithelial cell lining of the stomach. The adhesin was found to be distributed all over the bacterial cell surfaces. Our results suggest that the SDS-replica labeling allows assessment of protein localization to distinct cell compartments and analysis of co-localization with neighboring membrane structures.

Place, publisher, year, edition, pages
2000. Vol. 48, no 6, 877-883 p.
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:liu:diva-26007DOI: 10.1177/002215540004800616Local ID: 10460OAI: oai:DiVA.org:liu-26007DiVA: diva2:246555
Available from: 2009-10-08 Created: 2009-10-08 Last updated: 2017-12-13Bibliographically approved
In thesis
1. Characterisation of surface traits of Helicobacter pylori and their role in the infectious process
Open this publication in new window or tab >>Characterisation of surface traits of Helicobacter pylori and their role in the infectious process
2003 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The surface appendages of bacteria determine the initial contact with host cells. Characterisation of functional organisation and spatial distribution of adhesive traits of outer membrane components of Gram-negative bacteria is a key issue in studies of the parasite-host cell interaction.

With focus on the enteropathogenic Helicobacter pylori, evidenced to cause chronic gastric infections in humans, detergent-digested freeze fracture replica labelling was applied for ultrastructural analyses of envelope distribution of the virulence factors blood group antigen binding adhesin (BabA), and the carbonic anhydrases (α-CA, ß-CA). In a preliminary study the methodology was also used to study the bacteria-host contact between phagocytosing human neutrophils and wild-type H. pylori.

In parallel, bacterial traits were analysed from a molecular and biochemical perspective. This included the specific roles of the BabA and the sialic acid-binding adhesin (SabA), and the neutrophil activating protein (HP-NAP) in neutrophilic stimulation and subsequent inflammatory process. It was concluded that SabA is crucial in the initiation of a neutrophilic response in the mediated inflammation.

This thesis has demonstrated the synergistic application of ultrastructural, molecular and cellular microbiology tools for delineating complex patterns in bacteria-host interactions, thus utilising the well-characterised and clinically important human pathogen H. pylori. This approach could be applicable to other Gram-negative species to clarify known and discern new virulence mechanisms in the multifaceted field of bacterial pathogenesis and bacterial interactions with human host cells.

Place, publisher, year, edition, pages
Linköping: Linköpings universitet, 2003. 77 p.
Series
Linköping University Medical Dissertations, ISSN 0345-0082 ; 805
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-26665 (URN)11231 (Local ID)91-7373-490-X (ISBN)11231 (Archive number)11231 (OAI)
Public defence
2003-10-03, Elsa Brändströmsalen, Hälsouniversitetet, Linköping, 09:00 (Swedish)
Opponent
Available from: 2009-10-08 Created: 2009-10-08 Last updated: 2012-10-15Bibliographically approved

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Petersson, ChristofferLarsson, BertilMagnusson, Karl-Eric

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